ID CYAA_ANACY STANDARD; PRT; 502 AA. AC P43524; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-NOV-1995 (Rel. 32, Last annotation update) DE ADENYLATE CYCLASE (EC 4.6.1.1) (ATP PYROPHOSPHATE-LYASE) (ADENYLYL DE CYCLASE). OS Anabaena cylindrica. OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=IAM M-1; RX MEDLINE; 95325334. RA Katayama M., Wada Y., Ohmori M.; RT "Molecular cloning of the cyanobacterial adenylate cyclase gene from RT the filamentous cyanobacterium Anabaena cylindrica."; RL J. Bacteriol. 177:3873-3878(1995). CC -!- FUNCTION: MAY FUNCTION AS A MEMBRANE-LOCALIZED RECEPTOR PROTEIN. CC -!- CATALYTIC ACTIVITY: ATP = 3',5'-CYCLIC AMP + PYROPHOSPHATE. CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. THYLAKOID CC MEMBRANE. CC -!- DOMAIN: THE AMINO-TERMINAL HALF COULD SENSE SIGNALS SUCH AS PH OR CC A CHANGE IN MEMBRANE POTENTIAL AND REGULATES THE CATALYTIC CC ACTIVITY OF THE CARBOXY-TERMINAL HALF. CC -!- SIMILARITY: BELONGS TO ADENYLYL CYCLASE CLASS-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D55650; BAA09511.1; -. DR HSSP; P19754; 1AWK. DR INTERPRO; IPR000658; -. DR PFAM; PF00672; DUF5; 1. KW Lyase; cAMP synthesis; Transmembrane; Thylakoid membrane. FT DOMAIN 1 25 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 26 46 POTENTIAL. FT DOMAIN 47 206 LUMENAL, THYLAKOID (POTENTIAL). FT TRANSMEM 207 227 POTENTIAL. FT DOMAIN 228 502 CYTOPLASMIC (POTENTIAL). FT DOMAIN 321 502 CATALYTIC. SQ SEQUENCE 502 AA; 55293 MW; C61023B37CD8C4E9 CRC64; MGDFCRRVDC KAMKFFALRS SIRTQIMAST TLLILALIGA IVTVWAKSES TLYHQEKLND AKILSKVLSS TYANEVSEEN WSQIRLNIDL LLRENEDFLY ALVSDSNQKN QIAASSPDEF QNNYIPDIVS LSVTNAAINS SEKTHVVETF ILRDIYFADK LRAKRGEKVM EVSSDIQTLS GRKLGKLRIG ISLRKVNLAV TNAVNQALVV GFAGLNIGWI CAYFLAQHLS DPVRRLQISV AKIAGGDLQH RADIHSRADE IGALATSVNE MSAALQISFN KLKKTLDSFE RFVPNKFISV IAPQGIENIE VGAASTRRMT ILFCDIRGYT SMSEAMEPIE IFRFLNDYLA CMGKAIDEAG GFIDKYIGDA IMALFDDGNT DCALHAAILM QQALDKFNDE RSMQTGKTGL PRISVGIGIH RGTVVMGTVG FTSRIDSTVI GDAVNVASRI EGLTKQYGCN ILITESVVRN LSCPESFSLR LIDKSVKVKG KDEAISIYEV KA //